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Information on EC 2.1.1.357 - [histone H3]-lysine36 N-dimethyltransferase
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2.1.1.357 [histone H3]-lysine36 N-dimethyltransferaseIUBMB Comments
This entry describes a group of metazoan enzymes that catalyse two successive methylations of lysine36 of histone H3 (H3K36), forming mono- and dimethylated forms. These modifications influence the binding of chromatin-associated proteins. Some enzymes can catalyse three methylations, forming a trimethylated form; these enzymes are classified under EC 2.1.1.359, [histone H3]-lysine36 N-trimethyltransferase.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
2
+
=
2
+
2
+
=
2
+
Synonyms
mmset, whsc1, metnase, whsc1l1, h3k36 methyltransferase, histone h3 lysine 36 methyltransferase, h3k36-specific methyltransferase, nuclear receptor-binding set domain protein 2, kmt3b, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ash1L
EC 2.1.1.43
-
-
formerly, part transferred
-
H3K36 methyltransferase
KMT3B
KMT3C
-
-
-
-
MMSET
NSD1
NSD2
SETMAR
Whsc1
KMT3B
-
-
-
-
NSD2
-
-
-
-
SETMAR
-
-
-
-
Whsc1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
-
S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
(1a)
-
-
-
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[histone H3]-L-lysine36 N6-dimethyltransferase
This entry describes a group of metazoan enzymes that catalyse two successive methylations of lysine36 of histone H3 (H3K36), forming mono- and dimethylated forms. These modifications influence the binding of chromatin-associated proteins. Some enzymes can catalyse three methylations, forming a trimethylated form; these enzymes are classified under EC 2.1.1.359, [histone H3]-lysine36 N-trimethyltransferase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
2 S-adenosyl-L-methionine + [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-homocysteine + nuclear factor-kappaB
?
NSD1 also methylates nonhistone proteins, including the p65 subunit of nuclear factor-kappaB at Lys218 and Lys221
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-methionine + chicken nucleosome
S-adenosyl-L-homocysteine + chicken nucleosome N6-methyl-L-lysine
-
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + histone H3(K36) N6-methyl-L-lysine
-
-
-
?
S-adenosyl-L-methionine + recombinant nucleosome
S-adenosyl-L-homocysteine + recombinant nucleosome N6-methyl-L-lysine
-
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
preferred reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
additional information
?
-
enzyme mono- and dimethylates H3K36 and is inactive with H3K4 as substrate. Nucleosome containing histone H3 mutant K36A or histone H3 peptide 18-44 are not substrates. Isoform SETD2 is able to trimethylate H3K36 in vitro
-
-
?
additional information
?
-
the catalytic domain does not methylate recombinant nucleosomes containing histone H3 K36A mutants
-
-
?
additional information
?
-
enzyme shows versatilitiy in substrate recognition. In a pan-methylation assay of histone H3, H3K4me3 and H3K27me3 species are preferably detected rather than me1 and me2 species, while H3K9-me1 and -me2 and H3K79-me1 and -me2 species are favored against me3 species. H3K36 appears to be the preferable in vitro substrate for NSD1-C-terminal domain. NSD1 shows mono-/tri-methylation of histone H4K20
-
-
-
additional information
?
-
the enzyme does not methylate free histone octamers or (H3-H4)2 tetramers bound to DNA
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
2 S-adenosyl-L-methionine + [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-homocysteine + nuclear factor-kappaB
?
NSD1 also methylates nonhistone proteins, including the p65 subunit of nuclear factor-kappaB at Lys218 and Lys221
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
additional information
?
-
the enzyme does not methylate free histone octamers or (H3-H4)2 tetramers bound to DNA
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
preferred reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
histone H3.3 K36M mutant protein
-
inhibits the H3K36 methyltransferases MMSET and SETD2
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0028
S-adenosyl-L-methionine
cosubstrate recombinant nucleosome, pH 9.0, 23°C
0.0038
S-adenosyl-L-methionine
cosubstrate chicken nucleosome, pH 9.0, 23°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000028
A-893
Homo sapiens
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
germline deletion of NSD2 causes Wolf-Hirschhorn syndrome, a developmental disorder characterized by craniofacial defects, growth retardation and microcephaly
malfunction
mutations in NSD1 cause Sotos syndrome, a condition of childhood overgrowth and intellectual disability
malfunction
-
NSD1 enzyme mutants are associated with Sotos syndrome, myelodysplastic syndrome and cancer. NSD2 enzyme mutants are associated with Wolf-Hirschhorn syndrome and multiple myeloma
malfunction
specific knockout of cardiac enzyme does not lead to ventricular remodelling
malfunction
the enzyme methylates Lys36 of histone H3 to promote the establishment of Hox gene expression by counteracting polycomb silencing
physiological function
ASH1L is a HOX gene activator and important transcriptional regulator during development
physiological function
NSD2 is an important developmental regulator and oncogene. ASH1L is a HOX gene activator and important transcriptional regulator during development. SMYD2 promotes cancer cell proliferation in head and neck squamous cell carcinoma and esophageal squamous-cell carcinoma. SETMAR protein is linked to cancer via its role in DNA repair. The tumor suppressor SETD3 is implicated in DNA replication and repair due to its interaction with proliferating cell nuclear antigen
physiological function
NSD2 is an important developmental regulator and oncogene. SMYD2 promotes cancer cell proliferation in head and neck squamous cell carcinoma and esophageal squamous-cell carcinoma. SETMAR protein is linked to cancer via its role in DNA repair. The tumor suppressor SETD3 is implicated in DNA replication and repair due to its interaction with proliferating cell nuclear antigen
physiological function
the enzyme enhances nonhomologous end-joining repair of, and survival after, DNA double-strand breaks
physiological function
the enzyme promotes ventricular remodelling mediated by the regulation of demethylation of [histone H3]-L-lysine36
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SETMR_BOVIN
306
0
34254
Swiss-Prot
other Location (Reliability: 1)
SETMR_HUMAN
684
0
78034
Swiss-Prot
other Location (Reliability: 1)
SETMR_MOUSE
309
0
34417
Swiss-Prot
other Location (Reliability: 1)
SETMR_RAT
315
0
35030
Swiss-Prot
other Location (Reliability: 1)
SMYDL_CAEEL
507
0
57399
Swiss-Prot
other Location (Reliability: 2)
MES4_CAEEL
898
0
100065
Swiss-Prot
other Location (Reliability: 1)
MES4_DROME
1427
0
159028
Swiss-Prot
other Location (Reliability: 1)
NSD1_HUMAN
2696
0
296652
Swiss-Prot
other Location (Reliability: 1)
NSD1_MOUSE
2588
0
284084
Swiss-Prot
other Location (Reliability: 2)
NSD2_HUMAN
1365
0
152258
Swiss-Prot
other Location (Reliability: 2)
NSD2_MOUSE
1365
0
152253
Swiss-Prot
other Location (Reliability: 3)
ATXR7_ARATH
1423
0
158663
Swiss-Prot
other Location (Reliability: 5)
A0A6J8AFI7_MYTCO
157
0
18376
TrEMBL
other Location (Reliability: 5)
A0A812E2U6_SEPPH
1396
0
156002
TrEMBL
other Location (Reliability: 3)
A0A7R8CX31_LEPSM
715
0
81770
TrEMBL
Secretory Pathway (Reliability: 3)
A0A7R8D5U5_LEPSM
109
0
12953
TrEMBL
other Location (Reliability: 2)
A0A7R8H0P3_LEPSM
239
0
27547
TrEMBL
other Location (Reliability: 2)
A0A817FEX4_LEPSM
192
0
22335
TrEMBL
other Location (Reliability: 2)
A0A7R8CXQ5_LEPSM
457
0
53475
TrEMBL
other Location (Reliability: 5)
A0A7R8H552_LEPSM
255
0
28905
TrEMBL
other Location (Reliability: 4)
A0A7R8D7A1_LEPSM
523
0
60508
TrEMBL
other Location (Reliability: 2)
A0A7R8CHY6_LEPSM
418
0
47783
TrEMBL
other Location (Reliability: 1)
A0A7R8CXR9_LEPSM
604
0
69349
TrEMBL
other Location (Reliability: 2)
A0A7R8HD08_LEPSM
441
0
50787
TrEMBL
other Location (Reliability: 5)
A0A7R8CLK0_LEPSM
452
0
51834
TrEMBL
other Location (Reliability: 2)
A0A7R8CAH3_LEPSM
253
0
29668
TrEMBL
other Location (Reliability: 2)
A0A7R8CJC6_LEPSM
416
0
48159
TrEMBL
other Location (Reliability: 3)
A0A7R8CQJ3_LEPSM
243
0
26934
TrEMBL
other Location (Reliability: 2)
A0A7R8H0D9_LEPSM
579
0
65404
TrEMBL
other Location (Reliability: 1)
A0A7R8CNE9_LEPSM
264
0
30197
TrEMBL
other Location (Reliability: 2)
A0A7R8D4V9_LEPSM
1298
0
145623
TrEMBL
other Location (Reliability: 4)
A0A812ER50_SEPPH
359
6
39712
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7R8CF44_LEPSM
551
0
63456
TrEMBL
other Location (Reliability: 3)
A0A7R8CIC7_LEPSM
505
0
58218
TrEMBL
other Location (Reliability: 1)
A0A812B7R7_SEPPH
467
0
53985
TrEMBL
other Location (Reliability: 2)
A0A7R8H6F5_LEPSM
509
0
59387
TrEMBL
other Location (Reliability: 1)
A0A7R8CEQ2_LEPSM
279
0
32058
TrEMBL
other Location (Reliability: 3)
A0A812BKV0_SEPPH
269
0
31323
TrEMBL
other Location (Reliability: 4)
A0A6J8E0Q9_MYTCO
317
0
36051
TrEMBL
other Location (Reliability: 2)
A0A7R8HC12_LEPSM
528
0
59856
TrEMBL
other Location (Reliability: 1)
A0A7R8CWI2_LEPSM
374
0
43944
TrEMBL
Mitochondrion (Reliability: 5)
A0A6J8ET49_MYTCO
194
0
23121
TrEMBL
other Location (Reliability: 2)
A0A7R8H766_LEPSM
231
0
26712
TrEMBL
Mitochondrion (Reliability: 2)
A0A7R8D1Q7_LEPSM
226
0
25699
TrEMBL
other Location (Reliability: 4)
A0A7R8H0P2_LEPSM
240
0
27745
TrEMBL
other Location (Reliability: 3)
A0A7R8CV37_LEPSM
478
0
54774
TrEMBL
other Location (Reliability: 1)
A0A812ATE7_SEPPH
155
0
18044
TrEMBL
other Location (Reliability: 2)
A0A7R8DCP7_LEPSM
390
0
45491
TrEMBL
other Location (Reliability: 2)
A0A7R8D9E7_LEPSM
501
0
57328
TrEMBL
other Location (Reliability: 2)
A0A812BN91_SEPPH
250
0
28584
TrEMBL
other Location (Reliability: 2)
A0A812E6Y8_SEPPH
1350
0
150923
TrEMBL
other Location (Reliability: 3)
A0A6J8D8G3_MYTCO
272
0
30739
TrEMBL
other Location (Reliability: 1)
A0A7R8CM96_LEPSM
428
0
49391
TrEMBL
other Location (Reliability: 2)
A0A817FD95_LEPSM
222
0
25548
TrEMBL
other Location (Reliability: 3)
A0A7R8D3J3_LEPSM
530
0
61108
TrEMBL
other Location (Reliability: 1)
A0A7R8D199_LEPSM
186
0
21232
TrEMBL
other Location (Reliability: 1)
A0A7R8CD55_LEPSM
502
0
57454
TrEMBL
other Location (Reliability: 1)
A0A812E5R2_SEPPH
1364
0
152129
TrEMBL
other Location (Reliability: 3)
A0A7R8D5L5_LEPSM
397
0
46941
TrEMBL
other Location (Reliability: 2)
A0A817FE71_LEPSM
338
0
39056
TrEMBL
other Location (Reliability: 5)
A0A7R8CYX1_LEPSM
932
0
103799
TrEMBL
other Location (Reliability: 2)
ASH1L_HUMAN
2969
0
332790
Swiss-Prot
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain, in 0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, and 25% (w/v) PEG 3350 at 20°C
molecular modelling of the open-and-closed conformation of the catalytic domain
the SET domain is composed of three groups of canonical beta-sheets arranged in a triangular fashion with a group of two beta-sheets closely neighboring a conserved alpha-helix defining a cleft for the binding to the histone-tail ligand. The cofactor AdoMet and substrate bind at two adjacent sites to the SET domain. The histone-tail ligand binds into a groove formed by both the SET and postSET domains. The cofactor AdoMet binds into a distinct pocket located on the other side of the SET domain and acts as a methyl group donor. Both AdoMet and the L-lysine-histone are connected through a narrow tunnel where the methyl group is channeled. In the structure of the peptide-less NSDx02SET domain, the postSET domain loop is extended on top of the histone binding site, which sterically prevents the binding of either H3K36 or H4K20 substrates. In the presence of ligand, a network of residues stabilizes the H4-peptide tail on the binding site
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography, Mono S cation exchange column chromatography, and Superdex S200 gel filtration
glutathione-Sepharose column chromatography and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
expression of NSDs via tagging with a human influenza hemagglutinin tag greatly improves the quality of the recombinant NSDs, resulting in more than 95% pure, stable, and active NSD-hemagglutinins, with an increase in production yield up to 22.4fold and up to 6.25 mg/l from LB Eschewrichia coli culture, and without further purification
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eram, M.S.; Kuznetsova, E.; Li, F.; Lima-Fernandes, E.; Kennedy, S.; Chau, I.; Arrowsmith, C.H.; Schapira, M.; Vedadi, M.
Kinetic characterization of human histone H3 lysine 36 methyltransferases, ASH1L and SETD2
Biochim. Biophys. Acta
1850
1842-1848
2015
Homo sapiens (Q9NR48)
brenda
Rogawski, D.; Grembecka, J.; Cierpicki, T.
H3K36 methyltransferases as cancer drug targets Rationale and perspectives for inhibitor development
Future Med. Chem.
8
1589-1607
2016
Homo sapiens, Homo sapiens (Q96L73), Homo sapiens (Q9NR48)
-
brenda
Poulin, M.; Schneck, J.; Matico, R.; Hou, W.; McDevitt, P.; Holbert, M.; Schramm, V.
Nucleosome binding alters the substrate bonding environment of histone H3 lysine 36 methyltransferase NSD2
J. Am. Chem. Soc.
138
6699-6702
2016
Homo sapiens (Q96028)
brenda
Qiao, Q.; Li, Y.; Chen, Z.; Wang, M.; Reinberg, D.; Xu, R.
The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation
J. Biol. Chem.
286
8361-8368
2011
Homo sapiens (Q96L73)
brenda
Zhou, X.; Zhu, R.; Wu, X.; Xu, H.; Li, Y.; Xu, Q.; Liu, S.; Huang, H.; Xu, X.; Wan, L.; Wu, Q.; Liu, J.
NSD2 promotes ventricular remodelling mediated by the regulation of H3K36me2
J. Cell. Mol. Med.
23
568-575
2019
Mus musculus (Q8BVE8)
brenda
Wagner, E.; Carpenter, P.
Understanding the language of Lys36 methylation at histone H3
Nat. Rev. Mol. Cell Biol.
13
115-126
2012
Homo sapiens
brenda
Miyazaki, H.; Higashimoto, K.; Yada, Y.; Endo, T.A.; Sharif, J.; Komori, T.; Matsuda, M.; Koseki, Y.; Nakayama, M.; Soejima, H.; Handa, H.; Koseki, H.; Hirose, S.; Nishioka, K.
Ash1l methylates Lys36 of histone H3 independently of transcriptional elongation to counteract polycomb silencing
PLoS Genet.
9
e1003897
2013
Mus musculus (Q99MY8)
brenda
Fnu, S.; Williamson, E.; De Haro, L.; Brenneman, M.; Wray, J.; Shaheen, M.; Radhakrishnan, K.; Lee, S.; Nickoloff, J.; Hromasa, R.
Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining
Proc. Natl. Acad. Sci. USA
108
551-556
2011
Homo sapiens (Q53H47), Homo sapiens
brenda
Poulin, M.; Schneck, J.; Matico, R.; McDevitt, P.; Huddleston, M.; Hou, W.; Johnson, N.; Thrall, S.; Meek, T.; Schramm, V.
Transition state for the NSD2-catalyzed methylation of histone H3 lysine 36
Proc. Natl. Acad. Sci. USA
113
1197-1201
2016
Homo sapiens (O96028)
brenda
Fang, D.; Gan, H.; Lee, J.; Han, J.; Wang, Z.; Riester, S.; Jin, L.; Chen, J.; Zhou, H.; Wang, J.; Zhang, H.; Yang, N.; Bradley, E.; Ho, T.; Rubin, B.; Bridge, J.; Thibodeau, S.; Ordog, T.; Chen, Y.; Van Wijnen, A.; Oliveira, A.; Xu, R.; Westendorf, J.
The histone H3.3K36M mutation reprograms the epigenome of chondroblastomas
Science
352
1344-1348
2016
Homo sapiens
brenda
Morishita, M.; Di Luccio, E.
Structural insights into the regulation and the recognition of histone marks by the SET domain of NSD1
Biochem. Biophys. Res. Commun.
412
214-219
2011
Homo sapiens (Q96L73)
brenda
Morishita, M.; Mevius, D.; Di Luccio, E.
In vitro histone lysine methylation by NSD1, NSD2/MMSET/WHSC1 and NSD3/WHSC1L
BMC Struct. Biol.
14
25
2014
Homo sapiens (Q96L73)
brenda
Shen, Y.; Morishita, M.; di Luccio, E.
High yield recombinant expression and purification of oncogenic NSD1, NSD2, and NSD3 with human influenza hemagglutinin tag
Protein Expr. Purif.
166
105506
2020
Homo sapiens (Q96L73)
brenda
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Release 2023.1 (January 2023)
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